TY  - JOUR
A1  - Kreft, Jürgen
A1  - Funke, Dorothee
A1  - Haas, Albert
A1  - Lottspeich, Friedrich
A1  - Goebel, Werner
T1  - Production, purification and characterization of hemolysins from Listeria ivanovii and Listeria monocytogenes Sv4b.
N2  - In culture supematants of both Listeria ivanovii and Listeria monocytogenes Sv4b, for the first time a hemolysin of molecular weight 58 kDa was identified, which had all the characteristics of an SH-activated cytolysin, and which was therefore identified as Iisteriolysin 0 (LLO). In the case of L. ivanovii a second major supematant protein of molecular weight 24 kDa co-purified with LLO. However, the function of this protein has to be determined. In culture supematants of L. ivanovii a sphingomyelinase and a Iecithinase activity could be detected, both enzymatic activities together contributing to the pronounced hemolysis caused by L. ivanovii. The N-tenninal amino acid sequences of LLO and the 24 kDa from L. ivanovii are shown.
KW  - Biologie
KW  - Hemolysin
KW  - Listeria
Y1  - 1989
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60545
ER  - 
TY  - JOUR
A1  - Haas, Albert
A1  - Brehm, Klaus
A1  - Kreft, Jürgen
A1  - Goebel, Werner
T1  - Cloning, characterization, and expression in Escherichia coli of a gene encoding Listeria seeligeri catalase, a bacterial enzyme highly homologous to mammalian catalases
N2  - A gene coding for catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase; EC 1.11.1.6) of the grain-positive bacterium Listeria seeligeri was cloned from a plasmid library of EcoRI-digested chromosomal DNA, with Escherichia coli DHSa as a host. The recombinant catalase was expressed in E. coli to an enzymatic activity approximately SO times that of the combined E. coli catalases. The nucleutide sequence was determined, and the deduced amino acid sequence revealed 43.2% amino acid sequence identity between bovine liver catalase and L. seeligeri catalase. Most of the amino acid residues which are involved in catalytic activity, the formation of the active center accession channel, and heme binding in bovine liver catalase were also present in L. seeligeri catalase at the corresponding positions. The recombinant protein contained 488 amino acid residues and had a calculated molecular weight of 55,869. The predicted isoelectric point was 5.0. Enzymatic and genetic analyses showed that there is most probably a single catalase of this type in L. seeligeri. A perfect 21-bp inverted repeat, which was highly homologous to previously reported binding sequences of the Fur (ferric uptake regulon) protein of E. coli, was detected next to the putative promoter region of tbe L. seeligeri catalase gene.
KW  - Biologie
Y1  - 1991
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60536
ER  - 
TY  - JOUR
A1  - Brehm, Klaus
A1  - Haas, Albert
A1  - Goebel, Werner
A1  - Kreft, Jürgen
T1  - A gene encoding a superoxide dismutase of the facultative intracellular bacterium Listeria monocytogenes
N2  - A gene (Imsod) encoding superoxide dismutase (SOD; EC 1.15.1.1) of the facultative intracellular pathogen, Listeria monocytogenes, was cloned by functional complementation of an SOD-deficient Escherichia coli mutant. The nucleotide sequence was determined and the deduced amino acid (aa) sequence (202 aa) showed close similarity to manganese-containing SOD's from other organisms. Subunits of the recombinant L. monocytogenes SOD (re-SOD) and of both E. coli SODs formed enzymatically active hybrid enzymes in vivo. DNA/DNA-hybridization experiments showed that this type of recombinant re-sod gene is conserved within the genus Listeria.
KW  - Biologie
Y1  - 1992
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60515
ER  - 
TY  - JOUR
A1  - Haas, Albert
A1  - Dumbsky, Martina
A1  - Kreft, Jürgen
T1  - Listeriolysin genes: complete sequence of ilo from Listeria ivanovii and of lso from Listeria seeligeri
N2  - The completc DNA scqucnccs coding for thc thiol-activated cytolysins from Listeria ivanovii, ivanolysin 0 (ILO) and for sccligerolysin 0 (LSO) from Listeria seeligeri have been dctermined. Thc deduced amino acid scquences revealed that: (i) the primary translation products comprise 528 (ILO) and 530 (LSO) amino acids. respectively. (ii) ILO contains two cysteines. LSO has a substitution in the conserved cysteine motif.
KW  - Biologie
KW  - Thiol-activated cytolysin
KW  - Listeriolysin O
KW  - Cysteine: motif
KW  - ( L. ivanovii )
KW  - ( L. selligeri)
Y1  - 1992
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60529
ER  -